- Bacterial-yeast consortium as an effective biocatalyst for biodegradation of sulphonated azo dye Reactive Red 198
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A novel bacterial-yeast consortium (Brevibacillus laterosporus and Galactomyces geotrichum) acts as a proficient biocatalyst. It decolorized 92% of sulphonated azo dye Reactive Red 198 (RR 198) within 18 h at a dye concentration of 50 mg L-1 as compared to 58 and 42% decolorization using Brevibacillus laterosporus and Galactomyces geotrichum alone, respectively, in the same experimental conditions (pH 7, 40 °C, in static condition). The cumulative action of enzymes such as veratryl alcohol oxidase, laccase, NADH-DCIP reductase and azoreductase in the consortium culture was responsible for dye degradation. Fourier transform infrared spectroscopy and high performance thin layer chromatography analysis of the dye and its extracted metabolites suggested the biotransformation of RR 198 into simple metabolites; whereas the biotransformation of the same by individual microorganisms was different than by consortial biodegradation. According to gas chromatography-mass spectroscopy studies, RR 198 was biotransformed into much simpler compounds such as (ethylsulfonyl)benzene and 1,3,5-triazine by the bacterial-yeast consortium. This metabolic fate of the dye was entirely different in consortium than when compared to individual microbial treatment. Single microbial species could lead to only partial mineralization of the intact dye molecule; whereas, nearly complete degradation of the dye molecule was achieved using the consortium culture. This study clearly suggests that the consortium has an enormous strength to catalyze RR 198 within a short period as compared to individual microbial cultures. This journal is
- Kurade, Mayur B.,Waghmode, Tatoba R.,Jadhav, Mital U.,Jeon, Byong-Hun,Govindwar, Sanjay P.
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- Design, Synthesis, and Characterization of Ogerin-Based Positive Allosteric Modulators for G Protein-Coupled Receptor 68 (GPR68)
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G protein-coupled receptor 68 (GPR68) is an understudied orphan G protein-coupled receptor (GPCR). It is expressed most abundantly in the brain, potentially playing important roles in learning and memory. Pharmacological studies with GPR68 have been hinde
- Yu, Xufen,Huang, Xi-Ping,Kenakin, Terry P.,Slocum, Samuel T.,Chen, Xin,Martini, Michael L.,Liu, Jing,Jin, Jian
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p. 7557 - 7574
(2019/09/09)
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- New phenoxytriazine compound or pharmaceutically acceptable salt thereof having inhibitory activity on Hsp90 and medical use thereof
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The present invention relates to a novel phenoxytriazine based compound having inhibitory activity on Hsp90, a pharmaceutically acceptable salt thereof, and a medical use thereof wherein the phenoxytriazine based compound has outstanding effects of inhibi
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Paragraph 0049; 0050; 0065-0071; 0081-0087
(2016/10/24)
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- Targeting the hydrophobic region of Hsp90's ATP binding pocket with novel 1,3,5-triazines
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Heat shock protein 90 (Hsp90) is a molecular chaperone that plays an important role in regulating the maturation and stabilization of many oncogenic proteins. In an attempt to discover a new class of Hsp90 inhibitors, a series of 1,3,5-triazine compounds were rationally designed, synthesized, and their biological activities were evaluated. Compound 3b was found to degrade Hsp90's client proteins of Her2, Met and Akt and to induce the expression level of Hsp70. The binding mode of 3b in the ATP-binding site of Hsp90 was predicted by the molecular docking.
- Lee, Taeho,Seo, Young Ho
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supporting information
p. 6427 - 6431
(2013/11/19)
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